Protein : Qrob_P0068320.2 Q. robur
Protein Identifier  ? Qrob_P0068320.2 Organism . Name  Quercus robur
Score  0.0 Score Type  egn
Protein Description  (M=1) PTHR11998:SF4 - CLATHRIN COAT ADAPTOR AP3 MEDIUM CHAIN Gene Prediction Quality  validated
Protein length 

Sequence

Length: 74  
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0 Synonyms

4 GO Terms

Identifier Name Description
GO:0005515 protein binding Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
GO:0006886 intracellular protein transport The directed movement of proteins in a cell, including the movement of proteins between specific compartments or structures within a cell, such as organelles of a eukaryotic cell.
GO:0016192 vesicle-mediated transport A cellular transport process in which transported substances are moved in membrane-bounded vesicles; transported substances are enclosed in the vesicle lumen or located in the vesicle membrane. The process begins with a step that directs a substance to the forming vesicle, and includes vesicle budding and coating. Vesicles are then targeted to, and fuse with, an acceptor membrane.
GO:0030131 clathrin adaptor complex A membrane coat adaptor complex that links clathrin to a membrane.

28 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|tcc:TCM_026795 13 70 + 58 none 13.98 415 91.38 7e-30 Clathrin adaptor complexes medium subunit family protein isoform 1
blastp_kegg lcl|mdm:103451283 9 70 + 62 none 26.84 231 80.65 9e-30 AP-3 complex subunit mu-like
blastp_kegg lcl|pmum:103344380 13 70 + 58 none 13.98 415 91.38 1e-29 AP-3 complex subunit mu
blastp_kegg lcl|pper:PRUPE_ppa006358mg 13 70 + 58 none 13.98 415 91.38 1e-29 hypothetical protein
blastp_kegg lcl|fve:101305186 13 70 + 58 none 13.98 415 89.66 3e-29 AP-3 complex subunit mu-1-like
blastp_kegg lcl|mdm:103433853 13 70 + 58 none 13.98 415 86.21 5e-29 AP-3 complex subunit mu
blastp_kegg lcl|rcu:RCOM_1435740 13 70 + 58 none 13.98 415 86.21 6e-29 clathrin coat adaptor ap3 medium chain putative
blastp_kegg lcl|pxb:103930073 13 70 + 58 none 13.98 415 86.21 8e-29 AP-3 complex subunit mu
blastp_kegg lcl|pmum:103318889 14 71 + 58 none 27.10 214 87.93 1e-28 AP-3 complex subunit mu-like
blastp_kegg lcl|cmo:103502231 13 70 + 58 none 13.98 415 87.93 1e-28 AP-3 complex subunit mu
blastp_uniprot_sprot sp|F4I562|AP3M_ARATH 13 70 + 58 none 13.98 415 82.76 1e-28 AP-3 complex subunit mu OS Arabidopsis thaliana GN AP3M PE 1 SV 1
blastp_uniprot_sprot sp|P53678|AP3M2_RAT 13 70 + 58 none 13.88 418 55.17 2e-15 AP-3 complex subunit mu-2 OS Rattus norvegicus GN Ap3m2 PE 2 SV 1
blastp_uniprot_sprot sp|Q8R2R9|AP3M2_MOUSE 13 70 + 58 none 13.88 418 55.17 2e-15 AP-3 complex subunit mu-2 OS Mus musculus GN Ap3m2 PE 2 SV 1
blastp_uniprot_sprot sp|P53677|AP3M2_HUMAN 13 70 + 58 none 13.88 418 53.45 3e-15 AP-3 complex subunit mu-2 OS Homo sapiens GN AP3M2 PE 1 SV 1
blastp_uniprot_sprot sp|P47795|AP1M_DIPOM 13 70 + 58 none 13.88 418 53.45 5e-15 AP-1 complex subunit mu OS Diplobatis ommata PE 2 SV 1
blastp_uniprot_sprot sp|Q9GPF1|AP3M_DICDI 14 70 + 57 none 13.54 421 50.88 5e-15 AP-3 complex subunit mu OS Dictyostelium discoideum GN apm3 PE 2 SV 1
blastp_uniprot_sprot sp|P53676|AP3M1_RAT 13 70 + 58 none 13.88 418 51.72 1e-14 AP-3 complex subunit mu-1 OS Rattus norvegicus GN Ap3m1 PE 1 SV 1
blastp_uniprot_sprot sp|Q9JKC8|AP3M1_MOUSE 13 70 + 58 none 13.88 418 51.72 2e-14 AP-3 complex subunit mu-1 OS Mus musculus GN Ap3m1 PE 1 SV 1
blastp_uniprot_sprot sp|Q24K11|AP3M1_BOVIN 13 70 + 58 none 13.88 418 51.72 2e-14 AP-3 complex subunit mu-1 OS Bos taurus GN AP3M1 PE 2 SV 1
blastp_uniprot_sprot sp|Q5R478|AP3M1_PONAB 13 70 + 58 none 13.88 418 51.72 2e-14 AP-3 complex subunit mu-1 OS Pongo abelii GN AP3M1 PE 2 SV 1
rpsblast_cdd gnl|CDD|211363 6 71 + 66 none 26.61 248 46.97 2e-21 cd09252 AP-3_Mu3_Cterm C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes AP-1 AP-2 AP-3 and AP-4 described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4 respectively) a medium mu chain (mu1-4) and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 3 (AP-3) medium mu3 subunit which includes two closely related homologs mu3A (P47A encoded by ap3m1) and mu1B (P47B encoded by ap3m2). Mu3A is ubiquitously expressed but mu3B is specifically expressed in neurons and neuroendocrine cells. AP-3 is particularly important for targeting integral membrane proteins to lysosomes and lysome-related organelles at trans-Golgi network (TGN) and/or endosomes such as the yeast vacuole fly pigment granules and mammalian melanosomes platelet dense bodies and the secretory lysosomes of cytotoxic T lymphocytes. Unlike AP-1 and AP-2 which function in conjunction with clathrin which is a scaffolding protein participating in the formation of coated vesicles the nature of the outer shell of AP-3 containing coats remains to be elucidated. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi where Y is tyrosine X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu Ile Met Phe or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-3 mu3 subunit also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.
rpsblast_cdd gnl|CDD|211372 13 70 + 58 none 22.83 254 53.45 4e-15 cd09261 AP-3_Mu3B_Cterm C-terminal domain of medium Mu3B subunit in neuron-specific adaptor protein (AP) complex AP-3. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes AP-1 AP-2 AP-3 and AP-4 described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4 respectively) a medium mu chain (mu1-4) and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This subfamily corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 3 (AP-3) medium mu3B subunit encoded by ap3m2 gene. Mu3B is specifically expressed in neurons and neuroendocrine cells. Neuron-specific AP-3 appears to be involved in synaptic vesicle biogenesis from endosomes in neurons and plays an important role in synaptic transmission in the central nervous system. Unlike AP-1 and AP-2 which function in conjunction with clathrin which is a scaffolding protein participating in the formation of coated vesicles the nature of the outer shell of neuron-specific AP-3 containing coats remains to be elucidated. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi where Y is tyrosine X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu Ile Met Phe or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-3 mu3B subunit also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.
rpsblast_cdd gnl|CDD|211371 13 70 + 58 none 22.83 254 51.72 5e-14 cd09260 AP-3_Mu3A_Cterm C-terminal domain of medium Mu3A subunit in ubiquitously expressed adaptor protein (AP) complex AP-3. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes AP-1 AP-2 AP-3 and AP-4 described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4 respectively) a medium mu chain (mu1-4) and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This subfamily corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 3 (AP-3) medium mu3A subunit encoded by ap3m1gene. Mu3A is ubiquitously expressed in all mammalian tissues and cells. It appears to be localized to the trans-Golgi network (TGN) and/or endosomes and participates in trafficking to the vacuole/lysosome in yeast flies and mammals. Unlike AP-1 and AP-2 which function in conjunction with clathrin which is a scaffolding protein participating in the formation of coated vesicles the nature of the outer shell of ubiquitous AP-3 containing coats remains to be elucidated. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi where Y is tyrosine X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu Ile Met Phe or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-3 mu3A subunit also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.
rpsblast_cdd gnl|CDD|189773 14 71 + 58 Gaps:12 26.12 268 35.71 4e-13 pfam00928 Adap_comp_sub Adaptor complexes medium subunit family. This family also contains members which are coatomer subunits.
rpsblast_cdd gnl|CDD|211360 14 70 + 57 Gaps:3 25.10 239 45.00 3e-09 cd07954 AP_MHD_Cterm C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD). This family corresponds to the C-terminal domain of heterotetrameric AP complexes medium mu subunits and its homologs existing in monomeric stonins delta-subunit of the heteroheptameric coat protein I (delta-COPI) a protein encoded by a pro-death gene referred as MuD (also known as MUDENG mu-2 related death-inducing gene) an endocytic adaptor syp1 the mammalian FCH domain only proteins (FCHo1/2) SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1) and related proteins. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. Stonins have been characterized as clathrin-dependent AP-2 mu chain related factors and may act as cargo-specific sorting adaptors in endocytosis. Coat protein complex I (COPI)-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER and intra-Golgi transport. MuD is distantly related to the C-terminal domain of mu2 subunit of AP-2. It is able to induce cell death by itself and plays an important role in cell death in various tissues. Syp1 represents a novel type of endocytic adaptor protein that participates in endocytosis promotes vesicle tabulation and contributes to cell polarity and stress responses. It shares the same domain architecture with its two ubiquitously expressed mammalian counterparts FCHo1/2 which represent key initial proteins ultimately controlling cellular nutrient uptake receptor regulation and synaptic vesicle retrieval. They bind specifically to the plasma membrane and recruit the scaffold proteins eps15 and intersectin which subsequently engage the adaptor complex AP2 and clathrin leading to coated vesicle formation. Another mammalian neuronal-specific protein SGIP1 does have a C-terminal MHD and has been classified into this family as well. It is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis. It is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.
rpsblast_cdd gnl|CDD|211364 14 71 + 58 Gaps:14 26.57 271 30.56 1e-07 cd09253 AP-4_Mu4_Cterm C-terminal domain of medium Mu4 subunit in adaptor protein (AP) complex AP-4. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes AP-1 AP-2 AP-3 and AP-4 described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4 respectively) a medium mu chain (mu1-4) and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 4 (AP-4) medium mu4 subunit. AP-4 plays a role in signal-mediated trafficking of integral membrane proteins in mammalian cells. Unlike other AP complexes AP-4 is found only in mammals and plants. It is believed to be part of a nonclathrin coat since it might function independently of clathrin a scaffolding protein participating in the formation of coated vesicles. Recruitment of AP-4 to the trans-Golgi network (TGN) membrane is regulated by a small GTPase ADP-ribosylation factor 1 (ARF1) or a related protein. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. One of the most important sorting signals binding to mu subunits of AP complexes are tyrosine-based endocytotic signals which are of the form Y-X-X-Phi where Y is tyrosine X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu Ile Met Phe or Val. However AP-4 does not bind most canonical tyrosine-based signals except for two naturally occurring ones from the lysosomal membrane proteins CD63 and LAMP-2a. It binds YX [FYL][FL]E motif where X can be any residue from the cytosolic tails of amyloid precursor protein (APP) family members in a distinct way.
rpsblast_cdd gnl|CDD|211361 15 70 + 56 Gaps:14 26.12 268 30.00 4e-07 cd09250 AP-1_Mu1_Cterm C-terminal domain of medium Mu1 subunit in clathrin-associated adaptor protein (AP) complex AP-1. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes AP-1 AP-2 AP-3 and AP-4 described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4 respectively) a medium mu chain (mu1-4) and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 1 (AP-1) medium mu1 subunit which includes two closely related homologs mu1A (encoded by ap1m1) and mu1B (encoded by ap1m2). Mu1A is ubiquitously expressed but mu1B is expressed exclusively in polarized epithelial cells. AP-1 has been implicated in bi-directional transport between the trans-Golgi network (TGN) and endosomes. It plays an essential role in the formation of clathrin-coated vesicles (CCVs) from the trans-Golgi network (TGN). Epithelial cell-specific AP-1 is also involved in sorting to the basolateral surface of polarized epithelial cells. Recruitment of AP-1 to the TGN membrane is regulated by a small GTPase ADP-ribosylation factor 1 (ARF1). Phosphorylation/dephosphorylation events can also regulate the function of AP-1. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-1. Those cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi where Y is tyrosine X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu Ile Met Phe or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-1 mu1 subunit also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.
rpsblast_kog gnl|CDD|37951 14 70 + 57 none 13.64 418 63.16 1e-21 KOG2740 KOG2740 KOG2740 Clathrin-associated protein medium chain [Intracellular trafficking secretion and vesicular transport].

6 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 6 70 65 PTHR11998 none none none
PANTHER 6 70 65 PTHR11998:SF4 none none none
Gene3D 7 71 65 G3DSA:2.60.40.1170 none none none
Pfam 7 71 65 PF00928 none Adaptor complexes medium subunit family IPR008968
SUPERFAMILY 9 71 63 SSF49447 none none IPR028565
ProSiteProfiles 1 73 73 PS51072 none Mu homology domain (MHD) profile. IPR028565

0 Localization

0 Qtllist

0 Targeting